O08336 · CYPB_BACSU

  • Protein
    Bifunctional cytochrome P450/NADPH--P450 reductase 2
  • Gene
    cypB
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

FMN (UniProtKB | Rhea| CHEBI:58210 )

heme b (UniProtKB | Rhea| CHEBI:60344 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
165 μMlauric acid
542 μMmyristic acid
337 μMpalmitic acid
68.5 μMstearic acid
28.7 μMphytanic acid
68.3 μM15-methylpalmitic acid
79 μMarachidonic acid
5.1 μMNADPH
2.43 mMNADH
10.9 μMcytochrome cin the reductase assay
285 μMferricyanidein the reductase assay
kcat is 104 min-1 for lauric acid hydroxylation. kcat is 5556 min-1 for myristic acid hydroxylation. kcat is 676 min-1 for palmitic acid hydroxylation. kcat is 374 min-1 for stearic acid hydroxylation. kcat is 794 min-1 for phytanic acid hydroxylation. kcat is 3845 min-1 for 15-methylpalmitic acid hydroxylation. kcat is 1690 min-1 for arachidonic acid hydroxylation. kcat is 3520 min-1 for the reduction of cytochrome c. kcat is 37050 min-1 for the reduction of ferricyanide.

Features

Showing features for site, binding site.

TypeIDPosition(s)Description
Site271Important for catalytic activity
Binding site403Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue
Binding site492-497FMN (UniProtKB | ChEBI)
Binding site539-542FMN (UniProtKB | ChEBI)
Binding site573-575FMN (UniProtKB | ChEBI)
Binding site581-583FMN (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionaromatase activity
Molecular Functionfatty acid binding
Molecular Functionflavin adenine dinucleotide binding
Molecular FunctionFMN binding
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular FunctionNADPH-hemoprotein reductase activity
Molecular Functionoxidoreductase activity
Molecular Functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
Biological Processfatty acid oxidation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional cytochrome P450/NADPH--P450 reductase 2
  • Alternative names
    • CYP102A3
    • Fatty acid hydroxylase CypB
    • Flavocytochrome P450 102A3

Including 2 domains:

  • Recommended name
    Cytochrome P450 102A3
  • EC number
  • Recommended name
    NADPH--cytochrome P450 reductase
  • EC number

Gene names

    • Name
      cypB
    • Synonyms
      cyp102A3
      , yrhJ
    • Ordered locus names
      BSU27160

Organism names

Accessions

  • Primary accession
    O08336

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis89Hydroxylates shorter substrates with higher conversion rates than wild-type, and in contrast to wild-type, is also able to convert medium-chain alkanes and aromatic compounds; when associated with Q-190.
Mutagenesis190Hydroxylates shorter substrates with higher conversion rates than wild-type, and in contrast to wild-type, is also able to convert medium-chain alkanes and aromatic compounds; when associated with V-89.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000522071-1054Bifunctional cytochrome P450/NADPH--P450 reductase 2

Proteomic databases

Expression

Induction

Negatively regulated by the transcriptional repressor FatR (PubMed:11574077, PubMed:11734890).
Is induced by fatty acids such as oleate, linoleate and phytanate, that bind and displace the FatR repressor (PubMed:11734890).
Is also induced by palmitate, likely via another mechanism (PubMed:11574077).
Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969).

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-475Cytochrome P450
Compositional bias462-481Basic and acidic residues
Region462-482Disordered
Region476-1053NADPH--P450 reductase
Domain486-625Flavodoxin-like
Domain663-896FAD-binding FR-type

Sequence similarities

In the N-terminal section; belongs to the cytochrome P450 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,054
  • Mass (Da)
    118,676
  • Last updated
    1997-07-01 v1
  • Checksum
    705F8E27866CA110
MKQASAIPQPKTYGPLKNLPHLEKEQLSQSLWRIADELGPIFRFDFPGVSSVFVSGHNLVAEVCDEKRFDKNLGKGLQKVREFGGDGLFTSWTHEPNWQKAHRILLPSFSQKAMKGYHSMMLDIATQLIQKWSRLNPNEEIDVADDMTRLTLDTIGLCGFNYRFNSFYRDSQHPFITSMLRALKEAMNQSKRLGLQDKMMVKTKLQFQKDIEVMNSLVDRMIAERKANPDENIKDLLSLMLYAKDPVTGETLDDENIRYQIITFLIAGHETTSGLLSFAIYCLLTHPEKLKKAQEEADRVLTDDTPEYKQIQQLKYIRMVLNETLRLYPTAPAFSLYAKEDTVLGGEYPISKGQPVTVLIPKLHRDQNAWGPDAEDFRPERFEDPSSIPHHAYKPFGNGQRACIGMQFALQEATMVLGLVLKHFELINHTGYELKIKEALTIKPDDFKITVKPRKTAAINVQRKEQADIKAETKPKETKPKHGTPLLVLFGSNLGTAEGIAGELAAQGRQMGFTAETAPLDDYIGKLPEEGAVVIVTASYNGAPPDNAAGFVEWLKELEEGQLKGVSYAVFGCGNRSWASTYQRIPRLIDDMMKAKGASRLTAIGEGDAADDFESHRESWENRFWKETMDAFDINEIAQKEDRPSLSITFLSEATETPVAKAYGAFEGIVLENRELQTAASTRSTRHIELEIPAGKTYKEGDHIGILPKNSRELVQRVLSRFGLQSNHVIKVSGSAHMAHLPMDRPIKVVDLLSSYVELQEPASRLQLRELASYTVCPPHQKELEQLVSDDGIYKEQVLAKRLTMLDFLEDYPACEMPFERFLALLPSLKPRYYSISSSPKVHANIVSMTVGVVKASAWSGRGEYRGVASNYLAELNTGDAAACFIRTPQSGFQMPNDPETPMIMVGPGTGIAPFRGFIQARSVLKKEGSTLGEALLYFGCRRPDHDDLYREELDQAEQDGLVTIRRCYSRVENEPKGYVQHLLKQDTQKLMTLIEKGAHIYVCGDGSQMAPDVERTLRLAYEAEKAASQEESAVWLQKLQDQRRYVKDVWTGM

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias462-481Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U93874
EMBL· GenBank· DDBJ
AAB80867.1
EMBL· GenBank· DDBJ
Genomic DNA
AL009126
EMBL· GenBank· DDBJ
CAB14658.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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